Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum.
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Summary
A mutational analysis of the yeast ERO1 gene identifies two pairs of conserved cysteines likely to form redox-active disulfide bonds in Ero1p that engage directly in thiol-disulfide exchange with ER oxidoreductases.
- Type
- article
- Published
- 2000-09-01
- Cited by
- 121
- References
- 45
- Access
- Open access
- OpenAlex
- https://openalex.org/W2102837599
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:13908368
Keywords
Protein disulfide-isomerase, Oxidative folding, Endoplasmic reticulum, Biochemistry, Cysteine
References
- Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation.
- Electron avenue: pathways of disulfide bond formation and isomerization.
- Efficient site-directed mutagenesis using uracil-containing DNA.
- Methods in yeast genetics
- Competition between glutathione and protein thiols for disulphide-bond formation
- Recent developments in the field of iron‐sulfur proteins
- Yeast Saccharomyces cerevisiae selectable markers in pUC18 polylinkers
- Thioredoxin--a fold for all reasons.
- Selective retention of secretory proteins in the yeast endoplasmic reticulum by treatment of cells with a reducing agent
- The CXXC motif: a rheostat in the active site.
- Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase.
- 2.8-A structure of yeast serine carboxypeptidase.
- ERO1-L, a Human Protein That Favors Disulfide Bond Formation in the Endoplasmic Reticulum*
- A stable mixed disulfide between thioredoxin reductase and its substrate, thioredoxin: preparation and characterization.
- Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli.
- Identification of the three-dimensional thioredoxin motif: related structure in the ORF3 protein of the Staphylococcus aureus mer operon.
- Scanning and Escape during Protein-disulfide Isomerase-assisted Protein Folding*
- A pathway for disulfide bond formation in vivo.
- Reconstitution of a Protein Disulfide Catalytic System*
- The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity.
Cited by
- Steps in reductive activation of the disulfide‐generating enzyme Ero1p
- Les glutathion peroxydases et protéine disulfure isomérases de peuplier : potentialités du repliement thiorédoxine pour la catalyse des réactions redox
- PDI, Reactive oxygen species stress and Polyphenolic Phytochemicals: Implications for Neurodegenerative Diseases
- An investigation into the regulation of gene expression in response to ER stress
- Cell stress response and hypoxia in breast cancer
- Misfolded and dimeric HLA-B27 molecules : implication for Ankylosing Spondylitis
- The unfolded protein response and HLA-B27 misfolding : implications for ankylosing spondylitis.
- The mechanism of endoplasmic reticulum oxidoreductase 1 α (Ero1α) inactivation
- The role of PDI and ERp46 in oxidative protein folding in the endoplasmic reticulum
- Protein disulfide isomerase : function and mechanism in oxidative protein folding
- Scurvy leads to endoplasmic reticulum stress and apoptosis in the liver of Guinea pigs.
- Charakterisierung und Rekonstitution des Mia40-Erv1-Disulfidtransfersystems in Mitochondrien
- The Endoplasmic Reticulum: Folding, Calcium Homeostasis, Signaling, and Redox Control
- ERp57 binds competitively to protein disulfide isomerase and calreticulin.
- Mutations in the FAD Binding Domain Cause Stress-induced Misoxidation of the Endoplasmic Reticulum Oxidoreductase Ero1β*
- REACTIVE OXYGEN SPECIES, CELLULAR REDOX SYSTEMS AND APOPTOSIS
- Molecular Mechanisms Regulating Oxidative Activity of the Ero1 Family in the Endoplasmic Reticulum
- The dance of disulfide formation
- Ero1α Is Expressed on Blood Platelets in Association with Protein-disulfide Isomerase and Contributes to Redox-controlled Remodeling of αIIbβ3*
- Structure and Function of DsbA, a Key Bacterial Oxidative Folding Catalyst
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